Search Results
Overview
| Uniprot ID | Q9H0E9 |
|---|---|
| Protein Name | Bromodomain-containing protein 8 |
| Gene Name | BRD8 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 9 | ATGTGKHKLLSTGPT |
Function
May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Isoform 2 stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. At least isoform 1 and isoform 2 are components of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0097067 | cellular response to thyroid hormone stimulus |
| Cellular Component | GO:0035267 | NuA4 histone acetyltransferase complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000812 | Swr1 complex |
| Molecular Function | GO:0046966 | nuclear thyroid hormone receptor binding |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Biological Process | GO:0007166 | cell surface receptor signaling pathway |
| Biological Process | GO:0006325 | chromatin organization |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:1905168 | positive regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:2000779 | regulation of double-strand break repair |
Reference
[1] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.